Date published: 2025-9-6

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ARL11 Inhibitors

ARL11 inhibitors are chemical compounds that directly or indirectly influence the function of ARL11, a small GTPase known to regulate vesicle-mediated transport. Inhibitors such as Brefeldin A, Wortmannin, LY294002, Nocodazole, Vinblastine, Monensin, Chlorpromazine, Dynasore, Exo1, Pitstop 2, Latrunculin B, and Genistein can lead to the decreased functional activity of ARL11 through specific signaling pathways or biological processes that it is directly involved in. For instance, Brefeldin A inhibits protein transport from the endoplasmic reticulum to the Golgi apparatus, which can disrupt the formation and function of vesicles involved in ARL11-mediated transport. Wortmannin and LY294002, both PI3K inhibitors, can disrupt vesicle trafficking by inhibiting the PI3K-dependent pathway, a pathway that ARL11 is involved in.

Microtubule-disrupting agents such as Nocodazole and Vinblastine inhibit microtubule dynamics, leading to the disruption of vesicle transport along the microtubules, a process in which ARL11 is deeply involved. Monensin, a sodium ionophore, disrupts intracellular trafficking by altering ion gradients, a process that can disrupt the functional activity of ARL11. Chlorpromazine and Pitstop 2, both inhibitors of clathrin-mediated endocytosis, can also lead to decreased functional activity of ARL11 by disrupting vesicle-mediated transport. Dynasore and Exo1 inhibit the function of dynamin and the exocyst complex respectively, both crucial components in vesicle formation and trafficking, thereby leading to a decrease in ARL11's functional activity. Latrunculin B and Genistein, inhibitors of actin polymerization and tyrosine kinase respectively, can also disrupt intracellular processes leading to decreased ARL11 activity.

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